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Q5R880 (PLA2R_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Secretory phospholipase A2 receptor
Short name=PLA2-R
Short name=PLA2R
Alternative name(s):
180 kDa secretory phospholipase A2 receptor
M-type receptor

Cleaved into the following chain:

  1. Soluble secretory phospholipase A2 receptor
    Short name=Soluble PLA2-R
    Short name=Soluble PLA2R
Gene names
Name:PLA2R1
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

Protein attributes

Sequence length1464 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Receptor for secretory phospholipase A2 (sPLA2). Also able to bind to snake PA2-like toxins. Although its precise function remains unclear, binding of sPLA2 to its receptor participates in both positive and negative regulation of sPLA2 functions as well as clearance of sPLA2. Binding of sPLA2-IB/PLA2G1B induces various effects depending on the cell type, such as activation of the mitogen-activated protein kinase (MAPK) cascade to induce cell proliferation, the production of lipid mediators, selective release of arachidonic acid in bone marrow-derived mast cells. In neutrophils, binding of sPLA2-IB/PLA2G1B can activate p38 MAPK to stimulate elastase release and cell adhesion. May be involved in responses in proinflammatory cytokine productions during endotoxic shock. Also has endocytic properties and rapidly internalizes sPLA2 ligands, which is particularly important for the clearance of extracellular sPLA2s to protect their potent enzymatic activities. The soluble secretory phospholipase A2 receptor form is circulating and acts as a negative regulator of sPLA2 functions by blocking the biological functions of sPLA2-IB/PLA2G1B and sPLA2-X/PLA2G10 By similarity.

Subcellular location

Cell membrane; Single-pass type I membrane protein By similarity.

Soluble secretory phospholipase A2 receptor: Secreted By similarity.

Domain

C-type lectin domains 3-5 mediate the interaction with phospholipase PLA2G1B By similarity.

The endocytosis signal probably mediates endocytosis via clathrin-coated pits By similarity.

Post-translational modification

The secretory phospholipase A2 receptor form may be produced by the action of metalloproteinases. It contains all extracellular domains and only lacks transmembrane and cytosolic regions. It is however unclear whether this form is produced by proteolytic cleavage as suggested by some experiments, or by alternative splicing By similarity.

Sequence similarities

Contains 8 C-type lectin domains.

Contains 1 fibronectin type-II domain.

Contains 1 ricin B-type lectin domain.

Sequence caution

The sequence CAH92030.1 differs from that shown. Reason: Erroneous termination at position 1366. Translated as Gln.

Ontologies

Keywords
   Biological processEndocytosis
   Cellular componentCell membrane
Membrane
Secreted
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandLectin
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcytokine production

Inferred from sequence or structural similarity. Source: UniProtKB

oxidative stress-induced premature senescence

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of DNA damage response, signal transduction by p53 class mediator

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of arachidonic acid secretion

Inferred from sequence or structural similarity. Source: UniProtKB

reactive oxygen species metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

receptor-mediated endocytosis

Inferred from sequence or structural similarity. Source: UniProtKB

replicative senescence

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functioncarbohydrate binding

Inferred from electronic annotation. Source: InterPro

phospholipase binding

Inferred from sequence or structural similarity. Source: UniProtKB

receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 By similarity
Chain23 – 14641442Secretory phospholipase A2 receptor
PRO_0000311252
Chain23 – ?Soluble secretory phospholipase A2 receptor By similarityPRO_0000311253

Regions

Topological domain23 – 13981376Extracellular Potential
Transmembrane1399 – 141921Helical; Potential
Topological domain1420 – 146445Cytoplasmic Potential
Domain40 – 163124Ricin B-type lectin
Domain175 – 22349Fibronectin type-II
Domain240 – 357118C-type lectin 1
Domain387 – 504118C-type lectin 2
Domain524 – 645122C-type lectin 3
Domain675 – 799125C-type lectin 4
Domain821 – 940120C-type lectin 5
Domain967 – 1098132C-type lectin 6
Domain1123 – 1234112C-type lectin 7
Domain1259 – 1379121C-type lectin 8
Motif1437 – 14437Endocytosis signal

Amino acid modifications

Glycosylation951N-linked (GlcNAc...) Potential
Glycosylation4561N-linked (GlcNAc...) Potential
Disulfide bond53 ↔ 66 By similarity
Disulfide bond91 ↔ 108 By similarity
Disulfide bond180 ↔ 206 By similarity
Disulfide bond194 ↔ 221 By similarity
Disulfide bond262 ↔ 356 By similarity
Disulfide bond332 ↔ 348 By similarity
Disulfide bond408 ↔ 503 By similarity
Disulfide bond480 ↔ 495 By similarity
Disulfide bond619 ↔ 636 By similarity
Disulfide bond701 ↔ 798 By similarity
Disulfide bond776 ↔ 790 By similarity
Disulfide bond842 ↔ 939 By similarity
Disulfide bond916 ↔ 931 By similarity
Disulfide bond1069 ↔ 1089 By similarity
Disulfide bond1211 ↔ 1225 By similarity
Disulfide bond1282 ↔ 1378 By similarity
Disulfide bond1356 ↔ 1370 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5R880 [UniParc].

Last modified November 13, 2007. Version 2.
Checksum: 8D4DEA5A43CB1C8A

FASTA1,464168,437
        10         20         30         40         50         60 
MLLSPSLLLP LLLLLGAPRG CAEGVAAALT PERLLEWQDK GIFVIQSESL KKCIQAGKSV 

        70         80         90        100        110        120 
LTLENCKQAN KHMLWKWVSN HGLFNIGGSG CLGLNFSAPE QPLSLYECDS TLVSLRWRCD 

       130        140        150        160        170        180 
RKMITGPLQY SVQVAHDNTV VASRKYFHKW ISYGSGGGDI CEYLHKDLHT IKGNAHGMPC 

       190        200        210        220        230        240 
MFPFQYNHQW HHECTREGRE DDLLWCATTS RYERDEKWGF CPDPTSAEVG CDTIWEKDLN 

       250        260        270        280        290        300 
SHICYQFNLL SSLSWSEAHS SCQMQGGALL SITDETEENF IREHMSSKTV EVWMGLNQLD 

       310        320        330        340        350        360 
EHAGWQWSDG TPLNYLNWSP EVNFEPFVED HCGTFSSFIP SAWRSRDCAS TLPYVCKKYL 

       370        380        390        400        410        420 
NHIDHEIVEK DAWKYYATHC EPGWNPYNRN CYKLQKEEKT WHEALRSCQA DNSALIDITS 

       430        440        450        460        470        480 
LAEVEFLVTL LGDENASETW IGLSSNKIPV SFEWSNDSSV IFTNWHTLEP QIFPNRSQLC 

       490        500        510        520        530        540 
VSAEQSEGHW KVKNCEETLF YVCKKAGHVL SDAESGCQEG WERHGGFCYK IDTVLRSFDQ 

       550        560        570        580        590        600 
ASSGYYCPPA LVTITNRFEQ AFITSLIGSV VKMKDSYFWI ALQDQNDTGE YTWKPAGQKP 

       610        620        630        640        650        660 
EPVQYTHWNA HQPRYSGGCV AMRGRHPPGR WEVKHCRHFK AMSLCKQPVE NQEKAEYEER 

       670        680        690        700        710        720 
WPFHPCYLDW ESEPGLASCF KVFHSEKVLM KRTWREAEAF CEEFGAHLAS FAHIEEENFV 

       730        740        750        760        770        780 
NELLYSKFNW TEERQFWIGF NKRNPLNAGS WEWSDRIPVV SSFLDNNYFG EDARNCAVYK 

       790        800        810        820        830        840 
ANKTLLPLHC GSKREWICKI PRDVKPKIPF WYQYDVPWLF YQDAEYLFHT FASEWLNFEF 

       850        860        870        880        890        900 
VCSWLHSDLL TIHSAHEQEF IHSKIKALSK YGASWWIGLQ EERANDEFRW RDGTPVIYQN 

       910        920        930        940        950        960 
WDTGRERPVN NQSQRCGFIS SITGLWGSEE CSVSMPSICK RKKVLLIEKK KDTPKQHGTC 

       970        980        990       1000       1010       1020 
PKGWLYFNYK CLLLNIPKDP NSWKNWMHAQ HFCAEEGGTL VAIESEVEQA FITMNLFGQT 

      1030       1040       1050       1060       1070       1080 
TNVWIGLQND DYETWLNGKP VVYSNWSPFD IINIPSHNTT DVQKHIPLCA LLSSNPNFHF 

      1090       1100       1110       1120       1130       1140 
TGKWYFEDCG KEGYGFVCEK MQDTSGHGVN TSDMYPMPNT LEYGNRTYKI INANMTWYAA 

      1150       1160       1170       1180       1190       1200 
IKTCLMHGTQ LVSITDQYHQ SFLTVVLNRL GYAHWIGLFT TDNGLNFDWS DGTKSSFTFW 

      1210       1220       1230       1240       1250       1260 
KDEESSLLGD CVFADTNGLW HSTACESFLQ GAICHVPPET RQSEHPELCS ETSIPWIKFK 

      1270       1280       1290       1300       1310       1320 
SNCYSFSTVL DRMSFEAAHE FCKKEGSNLL TIKDEAENAF LLEELFAFGS SVQMVWLNAQ 

      1330       1340       1350       1360       1370       1380 
FDGNNETIKW FDGTPTDQSN WGIRKPDTDY FKPHHCVALR IPEGLQLSLC QEKKGFICKM 

      1390       1400       1410       1420       1430       1440 
EADIRTAEEL PEKGPSHSII PLAVVLTLIV IVAICTLSFC IYKHNGGFFR RLAGFRNPYY 

      1450       1460 
PATNFSTVHL EENILISDLE KSDQ

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References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR859874 mRNA. Translation: CAH92030.1. Sequence problems.
RefSeqNP_001126180.1. NM_001132708.1.
UniGenePab.11399.

3D structure databases

ProteinModelPortalQ5R880.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100173143.
KEGGpon:100173143.

Organism-specific databases

CTD22925.

Phylogenomic databases

HOVERGENHBG108261.
InParanoidQ5R880.
KOK06560.

Family and domain databases

Gene3D2.10.10.10. 1 hit.
3.10.100.10. 8 hits.
InterProIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
IPR000562. FN_type2_col-bd.
IPR013806. Kringle-like.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamPF00040. fn2. 1 hit.
PF00059. Lectin_C. 8 hits.
[Graphical view]
SMARTSM00034. CLECT. 8 hits.
SM00059. FN2. 1 hit.
SM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMSSF56436. C-type_lectin_fold. 8 hits.
SSF57440. Kringle-like. 1 hit.
SSF50370. RicinB_like. 1 hit.
PROSITEPS00615. C_TYPE_LECTIN_1. 3 hits.
PS50041. C_TYPE_LECTIN_2. 8 hits.
PS00023. FN2_1. 1 hit.
PS51092. FN2_2. 1 hit.
PS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePLA2R_PONAB
AccessionPrimary (citable) accession number: Q5R880
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: November 13, 2007
Last modified: May 29, 2013
This is version 51 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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